메뉴 건너뛰기




Volumn 5, Issue , 2015, Pages

Structural models of intrinsically disordered and calcium-bound folded states of a protein adapted for secretion

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; INTRINSICALLY DISORDERED PROTEIN; PROTEIN; PROTEIN BINDING;

EID: 84942043262     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep14223     Document Type: Article
Times cited : (49)

References (48)
  • 1
    • 84926068561 scopus 로고    scopus 로고
    • Functional roles of transiently and intrinsically disordered regions within proteins
    • doi: 10.1111/febs.13202
    • Uversky, V. N. Functional roles of transiently and intrinsically disordered regions within proteins. FEBS J 282, 1182-1189, doi: 10.1111/febs.13202 (2015).
    • (2015) FEBS J , vol.282 , pp. 1182-1189
    • Uversky, V.N.1
  • 2
    • 84925114160 scopus 로고    scopus 로고
    • Intrinsically disordered proteins in cellular signalling and regulation
    • doi: 10.1038/nrm3920
    • Wright, P. E. and Dyson, H. J. Intrinsically disordered proteins in cellular signalling and regulation. Nat Rev Mol Cell Biol 16, 18-29, doi: 10.1038/nrm3920 (2015).
    • (2015) Nat Rev Mol Cell Biol , vol.16 , pp. 18-29
    • Wright, P.E.1    Dyson, H.J.2
  • 3
    • 0034467679 scopus 로고    scopus 로고
    • RTX toxin structure and function: A story of numerous anomalies and few analogies in toxin biology
    • Welch, R. A. RTX toxin structure and function: a story of numerous anomalies and few analogies in toxin biology. Current topics in microbiology and immunology 257, 85-111 (2001).
    • (2001) Current Topics in Microbiology and Immunology , vol.257 , pp. 85-111
    • Welch, R.A.1
  • 4
    • 78649358856 scopus 로고    scopus 로고
    • RTX proteins: A highly diverse family secreted by a common mechanism
    • doi: FMR231 [pii] 10.1111/j.1574-6976.2010.00231.x
    • Linhartova, I. et al. RTX proteins: a highly diverse family secreted by a common mechanism. FEMS Microbiol Rev 34, 1076-1112, doi: FMR231 [pii] 10.1111/j.1574-6976.2010.00231.x (2010).
    • (2010) FEMS Microbiol Rev , vol.34 , pp. 1076-1112
    • Linhartova, I.1
  • 5
    • 0027292152 scopus 로고
    • Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: A two-domain protein with a calcium binding parallel beta roll motif
    • Baumann, U., Wu, S., Flaherty, K. M. and McKay, D. B. Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: a two-domain protein with a calcium binding parallel beta roll motif. EMBO J 12, 3357-3364 (1993).
    • (1993) EMBO J , vol.12 , pp. 3357-3364
    • Baumann, U.1    Wu, S.2    Flaherty, K.M.3    McKay, D.B.4
  • 6
    • 0026816008 scopus 로고
    • Structural and functional relationships among the RTX toxin determinants of gram-negative bacteria
    • Coote, J. G. Structural and functional relationships among the RTX toxin determinants of gram-negative bacteria. FEMS Microbiol Rev 8, 137-161 (1992).
    • (1992) FEMS Microbiol Rev , vol.8 , pp. 137-161
    • Coote, J.G.1
  • 7
    • 8844241421 scopus 로고    scopus 로고
    • Type i secretion in gram-negative bacteria
    • Delepelaire, P. Type I secretion in gram-negative bacteria. Biochim Biophys Acta 1694, 149-161 (2004).
    • (2004) Biochim Biophys Acta , vol.1694 , pp. 149-161
    • Delepelaire, P.1
  • 8
    • 18844428872 scopus 로고    scopus 로고
    • Type 1 protein secretion in bacteria, the ABC-transporter dependent pathway (review)
    • Holland, I. B., Schmitt, L. and Young, J. Type 1 protein secretion in bacteria, the ABC-transporter dependent pathway (review). Mol Membr Biol 22, 29-39 (2005).
    • (2005) Mol Membr Biol , vol.22 , pp. 29-39
    • Holland, I.B.1    Schmitt, L.2    Young, J.3
  • 9
    • 0032586774 scopus 로고    scopus 로고
    • Bordatella pertussis adenylate cyclase: A toxin with multiple talents
    • Ladant, D. and Ullmann, A. Bordatella pertussis adenylate cyclase: a toxin with multiple talents. Trends in microbiology 7, 172-176 (1999).
    • (1999) Trends in Microbiology , vol.7 , pp. 172-176
    • Ladant, D.1    Ullmann, A.2
  • 10
    • 84908689374 scopus 로고    scopus 로고
    • Calcium, acylation, and molecular confinement favor folding of bordetella pertussis adenylate cyclase CyaA toxin into a monomeric and cytotoxic form
    • doi: 10.1074/jbc.M114.580852
    • Karst, J. C. et al. Calcium, Acylation, and Molecular Confinement Favor Folding of Bordetella pertussis Adenylate Cyclase CyaA Toxin into a Monomeric and Cytotoxic Form. J Biol Chem 289, 30702-30716, doi: 10.1074/jbc.M114.580852 (2014).
    • (2014) J Biol Chem , vol.289 , pp. 30702-30716
    • Karst, J.C.1
  • 11
    • 0023834146 scopus 로고
    • Interaction of Bordetella pertussis adenylate cyclase with calmodulin. Identification of two separated calmodulinbinding domains
    • Ladant, D. Interaction of Bordetella pertussis adenylate cyclase with calmodulin. Identification of two separated calmodulinbinding domains. J Biol Chem 263, 2612-2618 (1988).
    • (1988) J Biol Chem , vol.263 , pp. 2612-2618
    • Ladant, D.1
  • 12
    • 75349096080 scopus 로고    scopus 로고
    • Calmodulin-induced conformational and hydrodynamic changes in the catalytic domain of Bordetella pertussis adenylate cyclase toxin
    • doi: 10.1021/bi9016389
    • Karst, J. C. et al. Calmodulin-induced conformational and hydrodynamic changes in the catalytic domain of Bordetella pertussis adenylate cyclase toxin. Biochemistry 49, 318-328, doi: 10.1021/bi9016389 (2010).
    • (2010) Biochemistry , vol.49 , pp. 318-328
    • Karst, J.C.1
  • 13
    • 84858600993 scopus 로고    scopus 로고
    • Identification of a region that assists membrane insertion and translocation of the catalytic domain of Bordetella pertussis CyaA toxin
    • doi: 10.1074/jbc.M111.316166
    • Karst, J. C. et al. Identification of a region that assists membrane insertion and translocation of the catalytic domain of Bordetella pertussis CyaA toxin. J Biol Chem 287, 9200-9212, doi: 10.1074/jbc.M111.316166 (2012).
    • (2012) J Biol Chem , vol.287 , pp. 9200-9212
    • Karst, J.C.1
  • 14
    • 84887474923 scopus 로고    scopus 로고
    • Characterization of a membrane-active peptide from the Bordetella pertussis CyaA toxin
    • doi: 10.1074/jbc.M113.508838
    • Subrini, O. et al. Characterization of a membrane-active peptide from the Bordetella pertussis CyaA toxin. J Biol Chem 288, 32585-32598, doi: 10.1074/jbc.M113.508838 (2013).
    • (2013) J Biol Chem , vol.288 , pp. 32585-32598
    • Subrini, O.1
  • 15
    • 0028519151 scopus 로고
    • Internal lysine palmitoylation in adenylate cyclase toxin from Bordetella pertussis
    • Hackett, M., Guo, L., Shabanowitz, J., Hunt, D. F. and Hewlett, E. L. Internal lysine palmitoylation in adenylate cyclase toxin from Bordetella pertussis. Science 266, 433-435 (1994).
    • (1994) Science , vol.266 , pp. 433-435
    • Hackett, M.1    Guo, L.2    Shabanowitz, J.3    Hunt, D.F.4    Hewlett, E.L.5
  • 16
    • 0141866842 scopus 로고    scopus 로고
    • Interaction of Bordetella pertussis adenylate cyclase with CD11b/CD18: Role of toxin acylation and identification of the main integrin interaction domain
    • El-Azami-El-Idrissi, M. et al. Interaction of Bordetella pertussis adenylate cyclase with CD11b/CD18: Role of toxin acylation and identification of the main integrin interaction domain. J Biol Chem 278, 38514-38521 (2003).
    • (2003) J Biol Chem , vol.278 , pp. 38514-38521
    • El-Azami-El-Idrissi, M.1
  • 17
    • 0032895750 scopus 로고    scopus 로고
    • Characterization of the C-terminal domain essential for toxic activity of adenylate cyclase toxin
    • Bejerano, M., Nisan, I., Ludwig, A., Goebel, W. and Hanski, E. Characterization of the C-terminal domain essential for toxic activity of adenylate cyclase toxin. Molecular microbiology 31, 381-392 (1999).
    • (1999) Molecular Microbiology , vol.31 , pp. 381-392
    • Bejerano, M.1    Nisan, I.2    Ludwig, A.3    Goebel, W.4    Hanski, E.5
  • 18
    • 0028877021 scopus 로고
    • Interaction of calcium with Bordetella pertussis adenylate cyclase toxin. Characterization of multiple calcium-binding sites and calcium-induced conformational changes
    • Rose, T., Sebo, P., Bellalou, J. and Ladant, D. Interaction of calcium with Bordetella pertussis adenylate cyclase toxin. Characterization of multiple calcium-binding sites and calcium-induced conformational changes. J Biol Chem 270, 26370-26376 (1995).
    • (1995) J Biol Chem , vol.270 , pp. 26370-26376
    • Rose, T.1    Sebo, P.2    Bellalou, J.3    Ladant, D.4
  • 19
    • 33745224983 scopus 로고    scopus 로고
    • Structural and functional characterization of an essential RTX subdomain of Bordetella pertussis adenylate cyclase toxin
    • Bauche, C. et al. Structural and functional characterization of an essential RTX subdomain of Bordetella pertussis adenylate cyclase toxin. J Biol Chem 281, 16914-16926 (2006).
    • (2006) J Biol Chem , vol.281 , pp. 16914-16926
    • Bauche, C.1
  • 21
    • 59449107337 scopus 로고    scopus 로고
    • RTX calcium binding motifs are intrinsically disordered in the absence of calcium: Implication for protein secretion
    • Chenal, A., Guijarro, J. I., Raynal, B., Delepierre, M. and Ladant, D. RTX calcium binding motifs are intrinsically disordered in the absence of calcium: implication for protein secretion. J Biol Chem 284, 1781-1789 (2009).
    • (2009) J Biol Chem , vol.284 , pp. 1781-1789
    • Chenal, A.1    Guijarro, J.I.2    Raynal, B.3    Delepierre, M.4    Ladant, D.5
  • 22
    • 78649896548 scopus 로고    scopus 로고
    • Calcium-induced folding and stabilization of the intrinsically disordered RTX domain of the CyaA toxin
    • doi: 10.1016/j.bpj.2010.10.016
    • Chenal, A. et al. Calcium-induced folding and stabilization of the intrinsically disordered RTX domain of the CyaA toxin. Biophys J 99, 3744-3753, doi: 10.1016/j.bpj.2010.10.016 (2010).
    • (2010) Biophys J , vol.99 , pp. 3744-3753
    • Chenal, A.1
  • 23
    • 77349122288 scopus 로고    scopus 로고
    • Characterization of the regions involved in the calcium-induced folding of the intrinsically disordered RTX motifs from the bordetella pertussis adenylate cyclase toxin
    • doi: S0022-2836(10)00077-X [pii] 10.1016/j.jmb.2010.01.031
    • Sotomayor Perez, A. C. et al. Characterization of the regions involved in the calcium-induced folding of the intrinsically disordered RTX motifs from the bordetella pertussis adenylate cyclase toxin. Journal of molecular biology 397, 534-549, doi: S0022-2836(10)00077-X [pii] 10.1016/j.jmb.2010.01.031 (2010).
    • (2010) Journal of Molecular Biology , vol.397 , pp. 534-549
    • Sotomayor Perez, A.C.1
  • 24
    • 84882248932 scopus 로고    scopus 로고
    • Molecular crowding stabilizes both the intrinsically disordered calcium-free state and the folded calcium-bound state of a repeat in toxin (RTX) protein
    • doi: 10.1021/ja404790f
    • Sotomayor-Perez, A. C., Subrini, O., Hessel, A., Ladant, D. and Chenal, A. Molecular Crowding Stabilizes Both the Intrinsically Disordered Calcium-Free State and the Folded Calcium-Bound State of a Repeat in Toxin (RTX) Protein. Journal of the American Chemical Society 135, 11929-11934, doi: 10.1021/ja404790f (2013).
    • (2013) Journal of the American Chemical Society , vol.135 , pp. 11929-11934
    • Sotomayor-Perez, A.C.1    Subrini, O.2    Hessel, A.3    Ladant, D.4    Chenal, A.5
  • 25
    • 79955750874 scopus 로고    scopus 로고
    • Calcium-induced folding of intrinsically disordered repeat-in-toxin (RTX) motifs via changes of protein charges and oligomerization states
    • doi: M110.210393 [pii] 10.1074/jbc.M110.210393
    • Sotomayor-Perez, A. C., Ladant, D. and Chenal, A. Calcium-induced folding of intrinsically disordered repeat-in-toxin (RTX) motifs via changes of protein charges and oligomerization states. J Biol Chem 286, 16997-17004, doi: M110.210393 [pii] 10.1074/jbc.M110.210393 (2011).
    • (2011) J Biol Chem , vol.286 , pp. 16997-17004
    • Sotomayor-Perez, A.C.1    Ladant, D.2    Chenal, A.3
  • 26
    • 84921717213 scopus 로고    scopus 로고
    • Disorder-to-order transition in the CyaA toxin RTX domain: Implications for toxin secretion
    • doi: 10.3390/toxins7010001
    • Sotomayor-Perez, A. C., Ladant, D. and Chenal, A. Disorder-to-order transition in the CyaA toxin RTX domain: implications for toxin secretion. Toxins (Basel) 7, 1-20, doi: 10.3390/toxins7010001 (2015).
    • (2015) Toxins (Basel) , vol.7 , pp. 1-20
    • Sotomayor-Perez, A.C.1    Ladant, D.2    Chenal, A.3
  • 27
    • 84857132923 scopus 로고    scopus 로고
    • How random are intrinsically disordered proteins? A small angle scattering perspective
    • Receveur-Brechot, V. and Durand, D. How random are intrinsically disordered proteins? A small angle scattering perspective. Current Protein and Peptide Science 13, 55-75 (2012).
    • (2012) Current Protein and Peptide Science , vol.13 , pp. 55-75
    • Receveur-Brechot, V.1    Durand, D.2
  • 28
    • 84865347103 scopus 로고    scopus 로고
    • Analysis of intrinsically disordered proteins by small-angle X-ray scattering
    • doi: 10.1007/978-1-4614-3704-8-7
    • Bernado, P. and Svergun, D. I. Analysis of intrinsically disordered proteins by small-angle X-ray scattering. Methods in molecular biology 896, 107-122, doi: 10.1007/978-1-4614-3704-8-7 (2012).
    • (2012) Methods in Molecular Biology , vol.896 , pp. 107-122
    • Bernado, P.1    Svergun, D.I.2
  • 29
    • 72449188596 scopus 로고    scopus 로고
    • NADPH oxidase activator p67(phox) behaves in solution as a multidomain protein with semi-flexible linkers
    • Durand, D. et al. NADPH oxidase activator p67(phox) behaves in solution as a multidomain protein with semi-flexible linkers. J Struct Biol 169, 45-53 (2010).
    • (2010) J Struct Biol , vol.169 , pp. 45-53
    • Durand, D.1
  • 30
    • 77955216637 scopus 로고    scopus 로고
    • Proline-rich salivary proteins have extended conformations
    • doi: 10.1016/j.bpj.2010.04.050
    • Boze, H. et al. Proline-rich salivary proteins have extended conformations. Biophys J 99, 656-665, doi: 10.1016/j.bpj.2010.04.050 (2010).
    • (2010) Biophys J , vol.99 , pp. 656-665
    • Boze, H.1
  • 31
    • 66449096362 scopus 로고    scopus 로고
    • The family X DNA polymerase from Deinococcus radiodurans adopts a non-standard extended conformation
    • doi: 10.1074/jbc.M809342200
    • Leulliot, N. et al. The family X DNA polymerase from Deinococcus radiodurans adopts a non-standard extended conformation. J Biol Chem 284, 11992-11999, doi: 10.1074/jbc.M809342200 (2009).
    • (2009) J Biol Chem , vol.284 , pp. 11992-11999
    • Leulliot, N.1
  • 32
    • 34347112128 scopus 로고
    • Die Rontgenkleinwinkelstreuung von dichtgepackten kolloiden Systemen
    • Porod, G. Die Rontgenkleinwinkelstreuung von dichtgepackten kolloiden Systemen. Kolloid. Z. 124, 83-114. (1951).
    • (1951) Kolloid. Z. , vol.124 , pp. 83-114
    • Porod, G.1
  • 33
    • 0014240199 scopus 로고
    • Light scattering from wormlike chains with excluded volume effects
    • doi: 10.1002/bip.1968.360060814
    • Sharp, P. and Bloomfield, V. A. Light scattering from wormlike chains with excluded volume effects. Biopolymers 6, 1201-1211, doi: 10.1002/bip.1968.360060814 (1968).
    • (1968) Biopolymers , vol.6 , pp. 1201-1211
    • Sharp, P.1    Bloomfield, V.A.2
  • 34
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from X-ray solution scattering
    • doi: 10.1016/S0006-3495(01)76260-1
    • Svergun, D. I., Petoukhov, M. V. and Koch, M. H. Determination of domain structure of proteins from X-ray solution scattering. Biophys J 80, 2946-2953, doi: 10.1016/S0006-3495(01)76260-1 (2001).
    • (2001) Biophys J , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.3
  • 35
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low-resolution structural models
    • Kozin, M. B. and Svergun, D. I. Automated matching of high- and low-resolution structural models. J. Appl. Cryst. 34, 33-41. (2001).
    • (2001) J. Appl. Cryst. , vol.34 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2
  • 36
    • 33644761306 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for the analysis of protein dynamics
    • doi: 10.1002/mas.20064
    • Wales, T. E. and Engen, J. R. Hydrogen exchange mass spectrometry for the analysis of protein dynamics. Mass spectrometry reviews 25, 158-170, doi: 10.1002/mas.20064 (2006).
    • (2006) Mass Spectrometry Reviews , vol.25 , pp. 158-170
    • Wales, T.E.1    Engen, J.R.2
  • 37
    • 79951887389 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for studying protein structure and dynamics
    • doi: 10.1039/c0cs00113a
    • Konermann, L., Pan, J. and Liu, Y. H. Hydrogen exchange mass spectrometry for studying protein structure and dynamics. Chem Soc Rev 40, 1224-1234, doi: 10.1039/c0cs00113a (2011).
    • (2011) Chem Soc Rev , vol.40 , pp. 1224-1234
    • Konermann, L.1    Pan, J.2    Liu, Y.H.3
  • 38
    • 84906949563 scopus 로고    scopus 로고
    • Local transient unfolding of native state PAI-1 associated with serpin metastability
    • doi: 10.1002/anie.201402796
    • Trelle, M. B., Madsen, J. B., Andreasen, P. A. and Jorgensen, T. J. Local transient unfolding of native state PAI-1 associated with serpin metastability. Angew Chem Int Ed Engl 53, 9751-9754, doi: 10.1002/anie.201402796 (2014).
    • (2014) Angew Chem Int Ed Engl , vol.53 , pp. 9751-9754
    • Trelle, M.B.1    Madsen, J.B.2    Andreasen, P.A.3    Jorgensen, T.J.4
  • 39
    • 84924859480 scopus 로고    scopus 로고
    • Mapping residual structure in intrinsically disordered proteins at residue resolution using millisecond hydrogen/deuterium exchange and residue averaging
    • doi: 10.1007/s13361-014-1033-6
    • Keppel, T. R. and Weis, D. D. Mapping residual structure in intrinsically disordered proteins at residue resolution using millisecond hydrogen/deuterium exchange and residue averaging. Journal of the American Society for Mass Spectrometry 26, 547-554, doi: 10.1007/s13361-014-1033-6 (2015).
    • (2015) Journal of the American Society for Mass Spectrometry , vol.26 , pp. 547-554
    • Keppel, T.R.1    Weis, D.D.2
  • 40
    • 84878107864 scopus 로고    scopus 로고
    • Hydrogen-exchange mass spectrometry for the study of intrinsic disorder in proteins
    • doi: 10.1016/j.bbapap.2012.10.009
    • Balasubramaniam, D. and Komives, E. A. Hydrogen-exchange mass spectrometry for the study of intrinsic disorder in proteins. Biochim Biophys Acta 1834, 1202-1209, doi: 10.1016/j.bbapap.2012.10.009 (2013).
    • (2013) Biochim Biophys Acta , vol.1834 , pp. 1202-1209
    • Balasubramaniam, D.1    Komives, E.A.2
  • 41
    • 80053286819 scopus 로고    scopus 로고
    • Structure and function of MARTX toxins and other large repetitive RTX proteins
    • doi: 10.1146/annurev-micro-090110-102943
    • Satchell, K. J. Structure and function of MARTX toxins and other large repetitive RTX proteins. Annual review of microbiology 65, 71-90, doi: 10.1146/annurev-micro-090110-102943 (2011).
    • (2011) Annual Review of Microbiology , vol.65 , pp. 71-90
    • Satchell, K.J.1
  • 42
    • 0028027226 scopus 로고
    • Crystal structure of the 50 kDa metallo protease from Serratia marcescens
    • doi: 10.1006/jmbi.1994.1576
    • Baumann, U. Crystal structure of the 50 kDa metallo protease from Serratia marcescens. Journal of molecular biology 242, 244-251, doi: 10.1006/jmbi.1994.1576 (1994).
    • (1994) Journal of Molecular Biology , vol.242 , pp. 244-251
    • Baumann, U.1
  • 43
    • 0034708415 scopus 로고    scopus 로고
    • Folding of a synthetic parallel beta-roll protein
    • Lilie, H., Haehnel, W., Rudolph, R. and Baumann, U. Folding of a synthetic parallel beta-roll protein. FEBS letters 470, 173-177 (2000).
    • (2000) FEBS Letters , vol.470 , pp. 173-177
    • Lilie, H.1    Haehnel, W.2    Rudolph, R.3    Baumann, U.4
  • 44
    • 33646364570 scopus 로고    scopus 로고
    • NMR structure of the R-module: A parallel beta-roll subunit from an Azotobacter vinelandii mannuronan C-5 epimerase
    • doi: 10.1074/jbc.M510069200
    • Aachmann, F. L. et al. NMR structure of the R-module: a parallel beta-roll subunit from an Azotobacter vinelandii mannuronan C-5 epimerase. J Biol Chem 281, 7350-7356, doi: 10.1074/jbc.M510069200 (2006).
    • (2006) J Biol Chem , vol.281 , pp. 7350-7356
    • Aachmann, F.L.1
  • 45
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: A case study using the Phyre server
    • doi: 10.1038/nprot.2009.2
    • Kelley, L. A. and Sternberg, M. J. Protein structure prediction on the Web: a case study using the Phyre server. Nature protocols 4, 363-371, doi: 10.1038/nprot.2009.2 (2009).
    • (2009) Nature Protocols , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 46
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • doi: 10.1529/biophysj.105.064154
    • Petoukhov, M. V. and Svergun, D. I. Global rigid body modeling of macromolecular complexes against small-angle scattering data. Biophys J 89, 1237-1250, doi: 10.1529/biophysj.105.064154 (2005).
    • (2005) Biophys J , vol.89 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 47
    • 77950552976 scopus 로고    scopus 로고
    • The implementation of SOMO (SOlution MOdeller) in the UltraScan analytical ultracentrifugation data analysis suite: Enhanced capabilities allow the reliable hydrodynamic modeling of virtually any kind of biomacromolecule
    • doi: 10.1007/s00249-009-0418-0
    • Brookes, E., Demeler, B., Rosano, C. and Rocco, M. The implementation of SOMO (SOlution MOdeller) in the UltraScan analytical ultracentrifugation data analysis suite: enhanced capabilities allow the reliable hydrodynamic modeling of virtually any kind of biomacromolecule. Eur Biophys J 39, 423-435, doi: 10.1007/s00249-009-0418-0 (2010).
    • (2010) Eur Biophys J , vol.39 , pp. 423-435
    • Brookes, E.1    Demeler, B.2    Rosano, C.3    Rocco, M.4
  • 48
    • 3943108216 scopus 로고    scopus 로고
    • Structure and function of tolC: The bacterial exit duct for proteins and drugs
    • doi: 10.1146/annurev.biochem.73.011303.074104
    • Koronakis, V., Eswaran, J. and Hughes, C. Structure and function of tolC: The bacterial exit duct for proteins and drugs. Annu Rev Biochem 73, 467-489, doi: 10.1146/annurev.biochem.73.011303.074104 (2004).
    • (2004) Annu Rev Biochem , vol.73 , pp. 467-489
    • Koronakis, V.1    Eswaran, J.2    Hughes, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.